Abstract
FOR MANY YEARS AFTER ITS SYSTEMATIC morphological description by Farquhar and Palade in 1963 (7), the tight junction remained a puzzle. The freeze-fracture knife exposed anastomosing ridges in platinum/carbon replicas resembling the bones of ancient fossils, and, like fossils, provided few clues to living, breathing function. Speculation abounded about the true nature of the tight junction, with those favoring protein or lipid structures squared off in competing camps (14) while others counted strands and developed models, waiting for new breakthroughs (4). All of this began to change in 1986 with the identification of ZO-1 (15), proudly named as the first bona fide component of the zonula occludens, as tight junctions were formally bestowed by Farquhar and Palade (7). Enthusiasm was tempered, however, with the recognition that ZO-1 was not an integral membrane protein, but one that associated with the cytoplasmic face of the tight junction and thus could not account for the intercellular seal or the intramembrane ridges.
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